ArticleInternational journal of molecular sciences2025
Molecular Structure of the mRNA Export Factor Gle1 from
Article in International journal of molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Gle1 functions as a regulator of Dbp5, a DEAD-box-containing RNA helicase that is a component of the nuclear pore complex. In association with Gle1 and inositol hexakisphosphate (IP6), ADP-bound Dbp5 facilitates the release of RNA. The RNA-bound Dbp5 undergoes ATP hydrolysis and is activated by Gle1 in the presence of IP6. The formation of a ternary complex involving Dbp5, Gle1, and the nucleoporin Nup159 promotes ADP secretion and prevents RNA recombination. To date, several complex structures of Gle1 with its binding partners have been described; however, the structure of unbound Gle1 remains elusive. To investigate the structural features associated with complex formation, the crystal structure of N-terminally truncated Gle1 from
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